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2.5.1.34: 4-dimethylallyltryptophan synthase

This is an abbreviated version!
For detailed information about 4-dimethylallyltryptophan synthase, go to the full flat file.

Word Map on EC 2.5.1.34

Reaction

dimethylallyl diphosphate
+
L-tryptophan
=
diphosphate
 +
4-(3-methylbut-2-enyl)-L-tryptophan

Synonyms

4-(gamma,gamma-dimethylallyl)tryptophan synthase, 4-dimethylallyltryptophan synthase, 4-DMATS, 7-dimethylallyltryptophan synthase, 7-DMATS, C4-prenyltransferase, dimethylallyl-tryptophan synthase, dimethylallylpyrophosphate:L-tryptophan dimethylallyltransferase, dimethylallylpyrophosphate:tryptophan dimethylallyl transferase, dimethylallylpyrophosphate:tryptophan dimethylallyltransferase, dimethylallyltransferase, tryptophan, dimethylallyltryptophan synthase, dimethylallyltryptophan synthetase, DMAT synthase, DMAT synthetase, DMATS, DmaW, DmaW2, FgaPT2, IfgA, MaPT, Proq05g069320, tryptophan C4-prenyltransferase, tryptophan C4-prenyltransferase FgaPT2, tryptophan C4-PT

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.34 4-dimethylallyltryptophan synthase

Engineering

Engineering on EC 2.5.1.34 - 4-dimethylallyltryptophan synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E89Q
-
site-directed mutagenesis, the mutant shows a 400fold reduction in kcat compared to the wild-type enzyme
K174A
K174E
site-directed mutagenesis
K174F
site-directed mutagenesis, the FgaPT2 mutant shows a much higher catalytic activity toward L-tyrosine than L-tryptophan compared to the wild-type. The single mutation on the key amino acid switches the tryptophan C4-prenyltransferase to a tyrosine C3-prenylating enzyme
K174F/R244E
site-directed mutagenesis
K174Q
K174W
site-directed mutagenesis
K174Y
site-directed mutagenesis
M328L
site-directed mutagenesis, the FgaPT2 mutant shows increased activity with L-tyrosine compared to the wild-type enzyme
R244D
R244E
site-directed mutagenesis
R244L
with cyclo-D-Trp-L-Tyr the product yield is 28.2%, which is 2.8-fold of that of wild-type enzyme FgaPT2
R244N
R244Q
T102C
site-directed mutagenesis
T102G
site-directed mutagenesis
T102R
site-directed mutagenesis
T102S
site-directed mutagenesis
T102V
site-directed mutagenesis
Y398F
site-directed mutagenesis, the FgaPT2 mutant shows increased activity with L-tyrosine compared to the wild-type enzyme
I80F
-
the mutant enzyme shows similar catalytic ability as FgaPT2 toward cyclo-D-Trp-L-Tyr
-
R244D
-
the mutant enzyme accepts cyclo-D-Trp-L-Tyr much better than the wild-type enzyme (FgaPT2), product yield of 22.4% compared to 10% for wild-type enzyme. The mutant enzyme does not show activity toward tyrosine and comparable or lower activity with tryptophan than wild-type enzyme (FgaPT2)
-
R244L
-
with cyclo-D-Trp-L-Tyr the product yield is 28.2%, which is 2.8-fold of that of wild-type enzyme FgaPT2
-
R244N
-
the mutant enzyme accepts cyclo-D-Trp-L-Tyr much better than the wild-type enzyme (FgaPT2), product yield of 47.4% compared to 10% for wild-type enzyme. The mutant enzyme does not show activity toward tyrosine and comparable or lower activity with tryptophan than wild-type enzyme (FgaPT2)
-
R244Q
-
the mutant enzyme accepts cyclo-D-Trp-L-Tyr much better than the wild-type enzyme (FgaPT2), product yield of 44.1% compared to 10% for wild-type enzyme. The mutant enzyme does not show activity toward tyrosine and comparable or lower activity with tryptophan than wild-type enzyme (FgaPT2)
-
additional information